TSKA_XENLA
ID TSKA_XENLA Reviewed; 351 AA.
AC Q65YW8; Q32N68;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Tsukushi-A {ECO:0000305};
DE AltName: Full=Leucine-rich repeat-containing protein 54 {ECO:0000250|UniProtKB:Q8CBR6};
DE AltName: Full=X-TSK {ECO:0000303|PubMed:16319115};
DE Flags: Precursor;
GN Name=tsku.L {ECO:0000312|Xenbase:XB-GENE-866233};
GN Synonyms=lrrc54 {ECO:0000250|UniProtKB:Q8CBR6};
GN ORFNames=XELAEV_18014091mg {ECO:0000312|EMBL:OCT96413.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAD44778.1};
RN [1] {ECO:0000312|EMBL:BAD44778.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15363410; DOI=10.1016/j.devcel.2004.08.014;
RA Ohta K., Lupo G., Kuriyama S., Keynes R., Holt C.E., Harris W.A.,
RA Tanaka H., Ohnuma S.;
RT "Tsukushi functions as an organizer inducer by inhibition of BMP activity
RT in cooperation with chordin.";
RL Dev. Cell 7:347-358(2004).
RN [2] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [3] {ECO:0000312|EMBL:AAI08804.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAI08804.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BMP4 AND DLL1, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16319115; DOI=10.1242/dev.02178;
RA Kuriyama S., Lupo G., Ohta K., Ohnuma S., Harris W.A., Tanaka H.;
RT "Tsukushi controls ectodermal patterning and neural crest specification in
RT Xenopus by direct regulation of BMP4 and X-delta-1 activity.";
RL Development 133:75-88(2006).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FGF8 AND NODAL2, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17925852; DOI=10.1371/journal.pone.0001004;
RA Morris S.A., Almeida A.D., Tanaka H., Ohta K., Ohnuma S.;
RT "Tsukushi modulates Xnr2, FGF and BMP signaling: regulation of Xenopus germ
RT layer formation.";
RL PLoS ONE 2:e1004-e1004(2007).
CC -!- FUNCTION: Contributes to various developmental events through its
CC interactions with multiple signaling pathways (PubMed:15363410,
CC PubMed:16319115, PubMed:17925852). Dorsalizing factor which functions
CC as an inhibitor of bone morphogenetic proteins (BMP) during
CC gastrulation (PubMed:15363410, PubMed:16319115, PubMed:17925852).
CC Promotes dll1-dependent activation of Notch signaling and is required
CC for neural crest formation (PubMed:16319115). Induces endoderm and
CC dorsal mesoderm formation by enhancing nodal2/Xnr2 activity while
CC inhibiting ventrolateral mesoderm formation through inhibition of fgf8
CC (PubMed:17925852). {ECO:0000269|PubMed:15363410,
CC ECO:0000269|PubMed:16319115, ECO:0000269|PubMed:17925852}.
CC -!- SUBUNIT: Interacts with bmp4 (PubMed:16319115). Interacts with dll1
CC (via extracellular region) (PubMed:16319115). Interacts with fgf8;
CC inhibits fgf8 signaling (PubMed:17925852). Interacts with nodal2/Xnr2;
CC enhances nodal2 activity (PubMed:17925852).
CC {ECO:0000269|PubMed:16319115, ECO:0000269|PubMed:17925852}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q65Z91}.
CC -!- TISSUE SPECIFICITY: During embryogenesis, localized to the animal
CC hemisphere during late blastula and gastrula stages (PubMed:17925852).
CC At stage 10, expression is also detected around the dorsal blastopore
CC lip (PubMed:15363410, PubMed:17925852). Expressed in the mandibular
CC crest segment, branchial crest segment and differentiating somites at
CC stage 21/22 (PubMed:15363410). Expressed in the germ ring including the
CC shield at shield stage and in the tailbud at the 10-somite stage
CC (PubMed:15363410). At the early neurula stage (stage 13), expression is
CC hardly detectable in the presumptive neural plate region, and
CC restricted to the non-neural ectoderm where its levels increase by
CC stage 14, especially in the presumptive anterior neural fold
CC (PubMed:16319115). Also expressed in the prospective cranial neural
CC crest (PubMed:16319115). At the early tailbud stage (stage 23),
CC expressed in cranial neural crest cells, the dorsal retina and the lens
CC placode (PubMed:16319115). {ECO:0000269|PubMed:15363410,
CC ECO:0000269|PubMed:16319115, ECO:0000269|PubMed:17925852}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression peaks during germ layer
CC formation and early gastrulation. {ECO:0000269|PubMed:17925852}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown causes anterior neural
CC developmental defects (PubMed:15363410). Morpholino knockdown impairs
CC neural crest formation (PubMed:16319115). Morpholino knockdown results
CC in impaired endoderm formation and mesoderm patterning
CC (PubMed:17925852). {ECO:0000269|PubMed:15363410,
CC ECO:0000269|PubMed:16319115, ECO:0000269|PubMed:17925852}.
CC -!- MISCELLANEOUS: This factor is named 'Tsukushi' because its expression
CC pattern in chick embryos is similar to the shape of the Japanese
CC horsetail plant, tsukushi. {ECO:0000250|UniProtKB:Q65Z91}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB176536; BAD44778.1; -; mRNA.
DR EMBL; CM004468; OCT96413.1; -; Genomic_DNA.
DR EMBL; BC108803; AAI08804.1; -; mRNA.
DR RefSeq; NP_001088996.1; NM_001095527.1.
DR AlphaFoldDB; Q65YW8; -.
DR SMR; Q65YW8; -.
DR STRING; 8355.Q65YW8; -.
DR DNASU; 496379; -.
DR GeneID; 496379; -.
DR CTD; 496379; -.
DR Xenbase; XB-GENE-866233; tsku.L.
DR OMA; SQDVRCR; -.
DR OrthoDB; 1168051at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 496379; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0098868; P:bone growth; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 8.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW Developmental protein; Leucine-rich repeat; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..351
FT /note="Tsukushi-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5010506311"
FT REPEAT 59..82
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 85..108
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 109..132
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 134..155
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 158..181
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 182..203
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 204..226
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 252..276
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 277..300
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT CONFLICT 163
FT /note="T -> A (in Ref. 3; AAI08804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39027 MW; 5CCE0B250493257D CRC64;
MALSSWIFFL LVHGIVGGSR TCFPGCRCIV DNFGLFHSFS LTKVDCSRVG PHVVPVSIPL
DTSYLDLSSN RLKRINESVL SGPGYTTLMN LNLSYNQIVK ISYSTFSKLR YLESLDLSHN
LLETLPDGSF LYSRLTELDL SSNKIQKVGV GAFTLKSQGR SMTINLANNE IHSIFRGAER
PVPNIHSLML YGNQLLSVPD LHGIPLRHLN LDRNPLSKIE KVSFLGLESL THLSLSDLPN
LREVSPYSFK SLTSLLELDL SNNPNLKSLS SDMFFGLKAL QELNLAYSGV ASLPKDIMLH
LPSMKSITWG ENIRCLKTVK ESIFHAQKGR VRKEVLLCHD DNGAVPAQDI L
